Ex Parte Fixman et al

Board of Patent Appeals and Interferences

Jul 16, 2010

11575164 - (D) (B.P.A.I. Jul. 16, 2010)

UNITED STATES PATENT AND TRADEMARK OFFICE
____________________

BEFORE THE BOARD OF PATENT APPEALS
AND INTERFERENCES
___________________

Ex parte ELIZABETH D. FIXMAN
and
CHRISTINE T. MCCUSKER,
Appellants1
____________________

Appeal 2010-003592
Application 11/575,164
Technology Center 1600
____________________

Before CAROL A. SPIEGEL, FRANCISCO C. PRATS, and
JEFFREY N. FREDMAN, Administrative Patent Judges.

SPIEGEL, Administrative Patent Judge.

DECISION ON APPEAL2

1 The real party in interest is MCGILL UNIVERSITY (Amended Appeal
Brief filed 19 August 2009 ("App. Br.") at 1). This decision also cites to the
Examiner's Answer mailed 30 October 2009 ("Ans."), the Reply Brief filed
11 November 2009 ("Reply Br."), and the Specification of Application
11/575,164 ("Spec.")).
2 The two-month period for filing an appeal or commencing a civil action, as
recited in 37 C.F.R. § 1.304, or for filing a request for rehearing, as recited
in 37 C.F.R. § 41.52, begins to run from the "MAIL DATE" (paper delivery
mode) or the "NOTIFICATION DATE" (electronic delivery mode) shown
on the PTOL-90A cover letter attached to this decision.

Appeal 2010-003592
Application 11/575,164

Appellants appeal under 35 U.S.C. § 134(a) from an Examiner's final
rejection of all pending claims, claims 1-3. We have jurisdiction under 35
U.S.C. § 134. We REVERSE.
I. Statement of the Case
The subject matter on appeal relates to compositions and methods for
treating STAT-6 associated diseases or conditions.
STAT-6 is a member of the STAT (Signal Transducer and Activator
of Transcription) family of proteins that conveys (tranduces) a signal from a
receptor-JAK (Janus Kinase) complex to the DNA in the cell nucleus via
the "STAT pathway." In particular, cytokines IL-4 and IL-13 bind to cell
surface receptor IL-4Rα inducing activation of the receptor's associated JAK
kinase, which in turn phosphorylates specific tyrosine residues on the IL-
4Rα. Cytoplasmic STAT-6 is recruited to the phosphorylated receptor via
the STAT-6 SHG2 domain where STAT-6 itself is phosphorylated.
Phosphorylated STAT-6 dissociates from the receptor, homodimerizes, and
translocates to the nucleus where it regulates IL-4/IL-13-dependent gene
expression. [See Spec. 3:1-20.]
Claims 1-3 on appeal read as follows (App. Br. 17):
1. An isolated chimeric STAT-6 peptide
comprising a portion of a STAT-6 operably linked
to a protein transduction moiety, wherein said
portion of STAT-6 comprises Tyr-641 of SEQ ID
NO:24 or SEQ ID NO:25 and is 4 to 40 amino acid
residues in length.
2. The isolated chimeric STAT-6 peptide of
claim 1, wherein the portion of STAT-6 comprises
at least Tyr-641 of SEQ ID NO:24 or SEQ ID
NO:25 and the three amino acid residues
immediately C-terminal to Tyr-641.
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Appeal 2010-003592
Application 11/575,164

3. A method for treating a STAT-6 associated
disease or condition comprising administering an
effective amount of the isolated chimeric STAT-6
peptide of claim 1 to a subject having or at risk of
having allergic rhinitis, asthma or an immune
disorder associated with transcriptional activation
by STAT-6 dimer so that said allergic rhinitis,
asthma or immune disorder is treated.
The Examiner rejected claim 3 under 35 U.S.C. § 112, second
paragraph, as indefinite in reciting "a STAT-6 associated disease or
condition" (Ans. 3-4). The Examiner also rejected claims 1 and 2 under 35
U.S.C. § 102(b) as anticipated by Lu3 (id. at 4-5). In particular, the
Examiner found that Lu teaches a chimeric STAT6-Gal4 fusion protein (id.),
wherein Gal4 is protein transduction moiety which facilitates, enhances, or
increases intracellular transport of STAT-6 to the DNA (id. at 7-8).
Appellants argue that the Specification provides clear guidance and
enablement for treating subjects having or at risk of having a STAT-6
associated disease or condition, e.g., at page 22, lines 27-33, such that one
skilled in the art would be readily apprised of the scope of the claimed
invention (App. Br. 10; Reply Br. 3). Appellants further argue that the Gal4
portion of the Lu fusion protein is not a "protein transduction moiety" as
claimed because it facilitates delivery of STAT-6 to DNA, not into a cell
(App. Br. 12-15; Reply Br. 3-6).
Therefore, the dispositive issues in this appeal are whether the term "a
STAT-6 associated disease or condition" is indefinite as interpreted by one
of ordinary skill in the art in light of the instant Specification and whether

3 Lu et al., Identification of a STAT6 Domain Required for IL-4-Induced
Activation of Transcription, 159 THE JOURNAL OF IMMUNOLOGY 1255-1264
(1997) ("Lu").
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Appeal 2010-003592
Application 11/575,164

the Gal4 portion of Lu's chimeric STAT6-Gal4 fusion protein is a protein
transduction moiety as claimed.
II. Findings of Fact
The following findings of fact are supported by a preponderance of
the evidence of record.
[1] According to the Specification, since STAT-6 is an intracellular
protein, a protein transduction moiety is used to facilitate transport of
the STAT-6 peptide into target cells so that the STAT-6 peptide
sequences could bind to and inhibit wild-type STAT-6 protein in the
target cells (Spec. 6:30-7:8).
[2] Further according to the Specification, "[a] portion of STAT-6 is
intended to mean a peptide composed of at least Tyr-641 and the
three amino acid residues immediately C-terminal to Tyr-641 of the
native STAT-6 protein sequence, wherein Tyr-641 is phosphorylated
(*)" (Spec. 14:21-25).
[3] "[A] protein transduction moiety is any molecule which can be
operably attached to the STAT-6 peptide to facilitate, enhance, or
increase the intracellular transport or delivery of STAT-6 into a cell"
(Spec. 16:16-19).
[4] Exemplary protein transduction moieties suitable for delivering a
STAT-6 peptide into the cell include proteins that have been shown
to facilitate transport of proteins into the cell, e.g., HIV-1 Tat
transcription factor, arginine-rich peptides, e.g., a polylysine peptide
containing Tat PTD, Pep-1, or an HSP70 protein or fragment thereof
(Spec. 16:20-31).
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Appeal 2010-003592
Application 11/575,164

[5] In one aspect, an exemplary STAT-6 chimeric peptide may interfere
with dimerization of STAT-6 monomers, while in another aspect,
other chimeric STAT-6 peptides may inhibit tyrosine phosphorylation
(Spec. 13:20-14:8).
[6] According to the Specification,
[i]n addition to the treatment of allergic rhinitis or
asthma, the peptides disclosed herein will also be
useful in treating (i.e., suppressing or inhibiting)
the full spectrum of immune disorders which
require transcriptional activation by STAT-6
dimer, including allergic conditions (e.g., atopic
dermatitis, contact dermatitis, anaphylaxis, food or
drug induced allergy, conjunctivitis, uveitis,
hypersensitivity reactions, alveolitis and psoriasis),
Churg-Strauss syndrome, delayed-type
hypersensitivity, uriticaria, angiodema, eczema,
scleroderma, and systemic lupus erythematosus.
[Spec. 14:8-18.]
[7] Further according to the Specification,
[a]s many of the disease[s] or conditions
associated with STAT-6 involve individuals
predisposed to an allergen wherein subsequent
allergen exposure results in the signal transduction
cascade leading to STAT-6 activation, these
individuals, while not exhibiting signs or
symptoms, would have or be at risk of having a
STAT-6 associated disease or condition (Spec.
22:27-33).
[8] Lu generated fusion proteins wherein "[b]oth human (aa 629-847)
and murine (aa 596-837) STAT6 carboxyl-terminal region[s] were
fused to the Gal4 DNA binding and dimerization domain (aa 1-147)"
(Lu 1257, col. 1, ¶ 2).
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Appeal 2010-003592
Application 11/575,164

III. Discussion
A. Indefiniteness
Claims are definite if they
set out and circumscribe a particular area with a
reasonable degree of precision and particularity. It
is here where the definiteness of the language
employed must be analyzed- not in a vacuum, but
always in light of the teachings of the prior art and
of the particular application disclosure as it would
be interpreted by one possessing the ordinary level
of skill in the pertinent art.

In re Moore, 439 F.2d 1232, 1235 (CCPA 1971).
According to the Examiner, claim 3 is indefinite in reciting "a STAT-
6 associated disease or condition" (Ans. 3). However, the Specification
discloses specific diseases and conditions, e.g., allergic rhinitis or asthma
and immune disorders, including atopic dermatitis and hypersensitivity
reactions, and explains that these involve allergen exposure resulting in
STAT-6 transcriptional activation (FF 6, 7). The Examiner has failed to
explain why this disclosure would not have reasonably apprised one of
ordinary skill in the art of the scope and definition of "a STAT-6 associated
disease or condition." Moore, 439 F.2d at 1235. Therefore, we will not
sustain the rejection of claim 3 as indefinite under § 112, second paragraph.
B. Anticipation
Application claims are interpreted as broadly as is reasonable and
consistent with the specification, “taking into account whatever
enlightenment by way of definitions or otherwise that may be afforded by
the written description contained in the applicant's specification.” In re
Morris, 127 F.3d 1048, 1054 (Fed. Cir. 1997).
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Appeal 2010-003592
Application 11/575,164

Anticipation is a question of fact. In re Graves, 69 F.3d 1147, 1151
(Fed. Cir. 1995). Anticipation requires that a prior art reference describe
every limitation in a claim either explicitly or inherently. In re Schreiber,
128 F.3d 1473, 1477 (Fed. Cir. 1997).
According to the Examiner, the chimeric peptides of claims 1and 2 are
anticipated by the STAT6-Gal4 fusion proteins of Lu (Ans. 3-4).
Claims 1 and 2 recite a chimeric peptide comprising a protein
transduction moiety. The Specification expressly defines a protein
transduction moiety as "any molecule which can be operably attached to the
STAT-6 peptide to facilitate, enhance, or increase the intracellular transport
or delivery STAT-6 into a cell" (FF 3, emphasis added). Additionally, the
Specification describes using the protein transduction moiety to facilitate
transport of the STAT-6 peptide into target cells (FF 1) and exemplifies
protein transduction moieties suitable for delivering a STAT-6 peptide into
the cell (FF 4). The Examiner's interpretation of a protein transduction
moiety as a moiety, i.e., Gal4, that "facilitates, enhances, or increases
intracellular transport of STAT-6 to the DNA" (Ans. 8, original
emphasis) is inconsistent with the definition and written description of a
"protein transduction moiety" contained in Appellants' Specification.
Morris, 127 F.3d at 1054. Since the fusion protein of Lu does not contain a
protein transduction moiety as required by the chimeric peptide of claims 1
and 2, we will not sustain the rejection of these claims under § 102.
C. Conclusion
We reverse the rejection of claims 1 and 2 as anticipated by Lu
because the Gal4 portion of its STAT6-Gal4 fusion protein is a not protein
transduction moiety as claimed. We also reverse of claim 3 because the
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Appeal 2010-003592
Application 11/575,164

term "a STAT-6 associated disease or condition" as interpreted by one of
ordinary skill in the art in light of the instant Specification is not indefinite.
IV. Order
Upon consideration of the record, and for the reasons given, it is
ORDERED that the Examiner's decision to reject claims 1 and 2
under 35 U.S.C. § 102(b) as anticipated by Lu is REVERSED; and,
FURTHER ORDERED that the Examiner's decision to reject claim 3
under 35 U.S.C. § 112, second paragraph, as indefinite is REVERSED.
REVERSED

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